| IED ID | IndEnz0018001252 |
| Enzyme Type ID | peroxidase001252 |
| Protein Name |
Linoleate 10R-lipoxygenase EC 1.13.11.62 Cyclooxygenase-like fatty acid oxygenase Fatty acid oxygenase ppoC Linoleate 10R-dioxygenase 10R-DOX Psi-producing oxygenase C AfPpoC |
| Gene Name | ppoC AFUA_3G12120 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MLRRFSSTFKKKGDRESKQNGTASSSSAAVANTNNNDNKRHSKISAARKSSSDDDRNEKKGNSVSPFEKYASVLHASRSPIPNQTGDGAYLEHEHTTSLLQDARHLGFKDFKTLKEVIESKLPGGQLIDDKTMLMERIIQLVSRLPHNSKHREELTNAFLTELWDSLPHPPLSYMGNDYAYRSADGSNNNPTLPRLGAANTLYARTIPPLIIQPGGLPDPGLVFDTLFARQTFKPHPNKVSSVFFYWASLIIHDIFQTDYKNPNMNKTSGYLDLSILYGDVQEEQNLIRTFKDGKLKPDSFSEPRLQAFPATCCVLMVMLNRFHNYAVEQLAAINENGRFTKPADNLSEEEAKKAWAKYDEDLFQTGRLITCGLYINITLYDYLRTIVNLNRTNSTWCLDPRAQMEGSHTAPSGLGNQCSVEFNLAYRWHSATSATDEKWTEDVYERLMGKPASEVSMTELLMGLGKYQAELPKDPSKRTFADLERQADGRFKDEDLVNLLVNAVEDVAGSFGARNVPKVLKNVEILGIIQSRKWNVGSLNEFRKFFGLKPYETFEEINSDPDVAESLRSLYDHPDFVELYPGIVAEEAKQPMVPGVGIAPTYTISRAVLSDAVALVRGDRFYTIDYNPRNLTNWGYSEVRYDLSINQGCIFYKLATRAFPNWFKPDSIYAHYPMTIPSENRKIMKDLGREIHYSWDRPQYTPPRVDLVSYSNAKLVAEQQNQFRAAWGDTVEFVFGKASKEFKLYQDSAFIQKHADVMSKLLNKEEWHRSVKEFYEDITAKLLEDKTRRFGGINQVDITNDVGNLTPVIFAANVFSLPLKSKENPRGIYTEHEMFKVLAALYNCLYFDIDKTKSYPLHHASQAVGEPLGKALEANVKALGGSSLLSGIFRSFRENKNALKEYGVHLTKQLLENGLGAHEIAWAQFLPTVIAMVPAQAQAFTQIVDFYLSKEGSKHLPAIQRLAKQDTKKSDEQLLHYCLEAVRLNDMSGLYRQSETTLAVTDEAVEVTIQPGDKVFVSFAKANRDASVFPDPAEVRLDRPMNSYINPTLGPHGFLSKETSHIALTAMLRAVGRLNNLRVAPGVQGQLKKIPQPGGYSAYLREDHGSYSIFPTTFRVQYDA |
| Enzyme Length | 1121 |
| Uniprot Accession Number | Q4WY82 |
| Absorption | |
| Active Site | ACT_SITE 253; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate; Xref=Rhea:RHEA:31695, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:63324; EC=1.13.11.62; Evidence={ECO:0000269|PubMed:19289462}; |
| DNA Binding | |
| EC Number | 1.13.11.62 |
| Enzyme Function | FUNCTION: Responsible for the synthesis of various fatty acid-derived oxylipins. Oxidizes linoleic acid primarily to 10R-hydroperoxy-8,12-octadecadienoic acid (10R-HPODE) and, to a lesser extent, 8R-hydroperoxylinoleic acid (8R-HPODE). Also synthesizes 10-hydroxy-octadeca-8,12-dienoic acid (10-HODE) from linoleic acid and primarily 8R-hydroxy-octadeca-9-monoenoic acid (8-HOME, also known as psiB beta) from oleic acid. 8-HOME forms part of psi factor, a mixture of oxylipins that regulates the balance between sexual and asexual spore production. Displays epoxyalcohol synthase activity. Plays a role in the synthesis of prostaglandins which may be required for pathogenicity. {ECO:0000269|PubMed:16040966, ECO:0000269|PubMed:19289462}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Metal binding (5); Mutagenesis (7); Region (1); Sequence conflict (3); Site (1) |
| Keywords | Calcium;Dioxygenase;Fatty acid biosynthesis;Fatty acid metabolism;Hydrogen peroxide;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Oxidoreductase;Peroxidase;Prostaglandin biosynthesis;Prostaglandin metabolism;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 126,460 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.05 mM for linoleic acid {ECO:0000269|PubMed:19289462}; |
| Metal Binding | METAL 254; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 269; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 271; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 273; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 275; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:31695 |
| Cross Reference Brenda | 1.13.11.62; |